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Spectroscopic Characterization of the Isolated Iron–Molybdenum Cofactor (FeMoco) Precursor from the Protein NifEN

Authors

  • Aaron W. Fay,

    1. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697 (USA)
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    • These authors contributed equally to this work.

  • Michael A. Blank,

    1. Department of Chemistry, Stanford University, Stanford, CA 94305 (USA)
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    • These authors contributed equally to this work.

  • Chi Chung Lee,

    1. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697 (USA)
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  • Dr. Yilin Hu,

    Corresponding author
    1. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697 (USA)
    • Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697 (USA)
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  • Prof. Keith O. Hodgson,

    Corresponding author
    1. Department of Chemistry, Stanford University, Stanford, CA 94305 (USA)
    2. Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, CA 94025 (USA)
    • Department of Chemistry, Stanford University, Stanford, CA 94305 (USA)
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  • Prof. Britt Hedman,

    Corresponding author
    1. Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, CA 94025 (USA)
    • Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, CA 94025 (USA)
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  • Prof. Markus W. Ribbe

    Corresponding author
    1. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697 (USA)
    • Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697 (USA)
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  • This work was supported by Herman Frasch Foundation Grant 617-HF07 (M.W.R.), NIH Grant GM 67626 (M.W.R.), and NIH Grant RR 01209 (K.O.H.). SSRL operations are funded by the DOE BES, and the SSRL Structural Molecular Biology Program by NIH NCRR BTP and DOE BER.

Abstract

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Das aktive Zentrum der Mo-Nitrogenase ist der FeMo-Cofaktor (FeMoco). Nachdem eine FeMoco-Vorstufe auf NifEN, einem Gerüstprotein der FeMoco-Biosynthese abgefangen werden konnte, wurde sie nun von NifEN isoliert. Die beobachtete vollständige katalytische Aktivität nach Einbringen in Vorstufen-defiziente NifEN belegt die Unversehrtheit der isolierten Vorstufe. Eine XAS/EXAFS-Analysis stützt ein Modell mit acht Eisenzentren in der Vorstufe (siehe Struktur: Fe magenta, S gelb).

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